Crystal structure of l‐rhamnose 1‐dehydrogenase involved in the nonphosphorylative pathway of l‐rhamnose metabolism in bacteria. Issue 5 (5th February 2021)

• Record Type: Journal Article
• Authors: Yoshiwara, Kentaroh; Watanabe, Seiya; Watanabe, Yasunori
• Is Part Of: FEBS letters. Volume 595:Issue 5(2021)
• Page Start: 637
• Page End: 646
• Publication Date: 2021-02-05
• Subjects: aldose 1‐dehydrogenase -- crystal structure -- l‐rhamnose metabolism -- short‐chain dehydrogenase/reductase; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.14046
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Several microorganisms can utilize l ‐rhamnose as a carbon and energy source through the nonphosphorylative metabolic pathway, in which l ‐rhamnose 1‐dehydrogenase (RhaDH) catalyzes the NAD(P) + ‐dependent oxidization of l ‐rhamnose to l ‐rhamnono‐1, 4‐lactone. We herein investigated the crystal structures of RhaDH from Azotobacter vinelandii in ligand‐free, NAD + ‐bound, NADP + ‐bound, and l ‐rhamnose‐ and NAD + ‐bound forms at 1.9, 2.1, 2.4, and 1.6 Å resolution, respectively. The significant interactions with the 2′‐phosphate group of NADP +, but not the 2′‐hydroxyl group of NAD +, were consistent with a preference for NADP + over NAD + . The C5‐OH and C6‐methyl groups of l ‐rhamnose were recognized by specific residues of RhaDH through hydrogen bonds and hydrophobic contact, respectively, which contribute to the different substrate specificities from other aldose 1‐dehydrogenases in the short‐chain dehydrogenase/reductase superfamily. Abstract :